Human EDEM2 proteomics and glycoproteomics datasets

The endoplasmic reticulum (ER) homeostasis is maintained by redirecting misfolded or unfolded polypeptide products towards the endoplasmic reticulum associated degradation (ERAD), where proteins are sent to degradation in the ubiquitin-proteasome system. One active–player in this process, is EDEM2 (ER degradation-enhancing alpha-mannosidase-like protein 2), presumably to be one of the first ER mannosidases to act in the early steps of ERAD. Here, we provide a full data set encoding a proteomic, affinity-proteomic and glycoproteomic analysis of melanoma cells with altered expression level of EDEM2. Our affinity-proteomics data are complemented by molecular mass separation of the identified complexes in sucrose fractionation experiments, while the glycoproteomic results allowed the identification of new glycosylation sites regulated by EDEM2 altered expression level. These results were also validated by alternative biochemical methods.

内质网（endoplasmic reticulum, ER）稳态通过将错误折叠或未折叠的多肽产物定向转运至内质网相关降解（endoplasmic reticulum associated degradation, ERAD）通路得以维持，在此通路中蛋白质将通过泛素-蛋白酶体系统（ubiquitin-proteasome system）被降解。该过程的关键参与者之一为EDEM2（内质网降解增强型α-甘露糖苷酶样蛋白2，ER degradation-enhancing alpha-mannosidase-like protein 2），据推测其是最早在ERAD早期步骤发挥作用的内质网甘露糖苷酶之一。本研究提供了一套完整数据集，涵盖了EDEM2表达水平改变的黑色素瘤细胞的蛋白质组学（proteomic）、亲和蛋白质组学（affinity-proteomic）及糖蛋白质组学（glycoproteomic）分析内容。本研究的亲和蛋白质组学数据通过蔗糖分级分离实验中已鉴定复合物的分子质量分离结果得到补充，而糖蛋白质组学结果则成功鉴定出受EDEM2表达水平变化调控的新型糖基化位点。上述研究结果亦通过替代生化方法得到了验证。